메뉴 건너뛰기




Volumn 7, Issue 11, 2012, Pages

Exploring ORFan Domains in Giant Viruses: Structure of Mimivirus Sulfhydryl Oxidase R596

Author keywords

[No Author keywords available]

Indexed keywords

DISULFIDE; DITHIOL DERIVATIVE; DOUBLE STRANDED DNA; THIOL OXIDASE; UNCLASSIFIED DRUG; VIRUS ENZYME; VIRUS ENZYME R596;

EID: 84870344618     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0050649     Document Type: Article
Times cited : (15)

References (33)
  • 1
    • 34548419233 scopus 로고    scopus 로고
    • Unique genes in giant viruses: regular substitution pattern and anomalously short size
    • Ogata H, Claverie JM, (2007) Unique genes in giant viruses: regular substitution pattern and anomalously short size. Genome Res 17: 1353-1361.
    • (2007) Genome Res , vol.17 , pp. 1353-1361
    • Ogata, H.1    Claverie, J.M.2
  • 2
    • 0032871834 scopus 로고    scopus 로고
    • Finding families for genomic ORFans
    • Fischer D, Eisenberg D, (1999) Finding families for genomic ORFans. Bioinformatics 15: 759-762.
    • (1999) Bioinformatics , vol.15 , pp. 759-762
    • Fischer, D.1    Eisenberg, D.2
  • 3
    • 33751250835 scopus 로고    scopus 로고
    • Mimivirus giant particles incorporate a large fraction of anonymous and unique gene products
    • Renesto P, Abergel C, Decloquement P, Moinier D, Azza S, et al. (2006) Mimivirus giant particles incorporate a large fraction of anonymous and unique gene products. J Virol 80: 11678-11685.
    • (2006) J Virol , vol.80 , pp. 11678-11685
    • Renesto, P.1    Abergel, C.2    Decloquement, P.3    Moinier, D.4    Azza, S.5
  • 4
    • 41449101717 scopus 로고    scopus 로고
    • The Erv family of sulfhydryl oxidases
    • Fass D, (2008) The Erv family of sulfhydryl oxidases. Biochim Biophys Acta 1783: 557-566.
    • (2008) Biochim Biophys Acta , vol.1783 , pp. 557-566
    • Fass, D.1
  • 5
    • 0036142325 scopus 로고    scopus 로고
    • A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p
    • Gross E, Sevier CS, Vala A, Kaiser CA, Fass D, (2002) A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p. Nat Struct Bio. 9: 61-71.
    • (2002) Nat Struct Bio , vol.9 , pp. 61-71
    • Gross, E.1    Sevier, C.S.2    Vala, A.3    Kaiser, C.A.4    Fass, D.5
  • 6
    • 0037395242 scopus 로고    scopus 로고
    • The N-terminal cysteine pair of yeast sulfhydryl oxidase Erv1p is essential for in vivo activity and interacts with the primary redox centre
    • Hofhaus G, Lee JE, Tews I, Rosenberg B, Lisowsky T, (2003) The N-terminal cysteine pair of yeast sulfhydryl oxidase Erv1p is essential for in vivo activity and interacts with the primary redox centre. Eur J Biochem 270: 1528-1535.
    • (2003) Eur J Biochem , vol.270 , pp. 1528-1535
    • Hofhaus, G.1    Lee, J.E.2    Tews, I.3    Rosenberg, B.4    Lisowsky, T.5
  • 7
    • 80052452886 scopus 로고    scopus 로고
    • Structure of a baculovirus sulfhydryl oxidase, a highly divergent member of the Erv flavoenzyme family
    • Hakim M, Mandelbaum A, Fass D, (2011) Structure of a baculovirus sulfhydryl oxidase, a highly divergent member of the Erv flavoenzyme family. J Virol 85: 9406-9413.
    • (2011) J Virol , vol.85 , pp. 9406-9413
    • Hakim, M.1    Mandelbaum, A.2    Fass, D.3
  • 8
    • 77956312909 scopus 로고    scopus 로고
    • Cytosolic disulfide bond formation in cells infected with large nucleocytoplasmic DNA viruses
    • Hakim M, Fass D, (2010) Cytosolic disulfide bond formation in cells infected with large nucleocytoplasmic DNA viruses. Antioxid Redox Signal 13: 1261-1271.
    • (2010) Antioxid Redox Signal , vol.13 , pp. 1261-1271
    • Hakim, M.1    Fass, D.2
  • 9
    • 77956313447 scopus 로고    scopus 로고
    • Oxidative protein folding and the Quiescin-sulfhydryl oxidase family of flavoproteins
    • Kodali VK, Thorpe C, (2010) Oxidative protein folding and the Quiescin-sulfhydryl oxidase family of flavoproteins. Antioxid Redox Signal 13: 1217-1230.
    • (2010) Antioxid Redox Signal , vol.13 , pp. 1217-1230
    • Kodali, V.K.1    Thorpe, C.2
  • 10
    • 68149178656 scopus 로고    scopus 로고
    • Dimer interface migration in a viral sulfhydryl oxidase
    • Hakim M, Fass D, (2009) Dimer interface migration in a viral sulfhydryl oxidase. J Mol Biol 391: 758-768.
    • (2009) J Mol Biol , vol.391 , pp. 758-768
    • Hakim, M.1    Fass, D.2
  • 11
    • 78650627880 scopus 로고    scopus 로고
    • Giant virus with a remarkable complement of genes infects marine zooplankton
    • Fischer MG, Allen MJ, Wilson WH, Suttle CA, (2010) Giant virus with a remarkable complement of genes infects marine zooplankton. Proc Natl Acad Sci USA 107: 19508-19513.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 19508-19513
    • Fischer, M.G.1    Allen, M.J.2    Wilson, W.H.3    Suttle, C.A.4
  • 12
    • 80054814749 scopus 로고    scopus 로고
    • Distant Mimivirus relative with a larger genome highlights the fundamental features of Megaviridae
    • Arslan D, Legendre M, Seltzer V, Abergel C, Claverie JM, (2011) Distant Mimivirus relative with a larger genome highlights the fundamental features of Megaviridae. Proc Natl Acad Sci USA 108: 17486-17491.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 17486-17491
    • Arslan, D.1    Legendre, M.2    Seltzer, V.3    Abergel, C.4    Claverie, J.M.5
  • 13
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: conservation mapping in 3D
    • Holm L, Rosenström P, (2010) Dali server: conservation mapping in 3D. Nucl Acids Res 38: W545-W549.
    • (2010) Nucl Acids Res , vol.38
    • Holm, L.1    Rosenström, P.2
  • 14
    • 0344305738 scopus 로고    scopus 로고
    • Exploring the sequence patterns in the α-helices of proteins
    • Wang J, Feng J-A, (2003) Exploring the sequence patterns in the α-helices of proteins. Prot Eng Des Sel 16: 799-807.
    • (2003) Prot Eng Des Sel , vol.16 , pp. 799-807
    • Wang, J.1    Feng, J.-A.2
  • 15
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones DT, (1999) Protein secondary structure prediction based on position-specific scoring matrices. J Mol Biol 292: 195-202.
    • (1999) J Mol Biol , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 16
    • 37349063372 scopus 로고    scopus 로고
    • Amino acid pairing at the N- and C-termini of helical segments in proteins
    • Fonseca NA, Camacho R, Magalhães AL, (2008) Amino acid pairing at the N- and C-termini of helical segments in proteins. Proteins 70: 188-196.
    • (2008) Proteins , vol.70 , pp. 188-196
    • Fonseca, N.A.1    Camacho, R.2    Magalhães, A.L.3
  • 17
    • 33747352990 scopus 로고    scopus 로고
    • Gain of function in an ERV/ALR sulfhydryl oxidase by molecular engineering of the shuttle disulfide
    • Vitu E, Bentzur M, Lisowsky T, Kaiser CA, Fass D, (2006) Gain of function in an ERV/ALR sulfhydryl oxidase by molecular engineering of the shuttle disulfide. J Mol Biol 362: 89-101.
    • (2006) J Mol Biol , vol.362 , pp. 89-101
    • Vitu, E.1    Bentzur, M.2    Lisowsky, T.3    Kaiser, C.A.4    Fass, D.5
  • 18
    • 28444436253 scopus 로고    scopus 로고
    • Structural determinants of substrate access to the disulfide oxidase Erv2p
    • Vala A, Sevier CS, Kaiser CA, (2005) Structural determinants of substrate access to the disulfide oxidase Erv2p. J Mol Biol 354: 952-966.
    • (2005) J Mol Biol , vol.354 , pp. 952-966
    • Vala, A.1    Sevier, C.S.2    Kaiser, C.A.3
  • 19
    • 77951857386 scopus 로고    scopus 로고
    • mRNA deep sequencing reveals 75 new genes and a complex transcriptional landscape in Mimivirus
    • Legendre M, Audic S, Poirot O, Hingamp P, Seltzer V, et al. (2010) mRNA deep sequencing reveals 75 new genes and a complex transcriptional landscape in Mimivirus. Genome Res 20: 664-674.
    • (2010) Genome Res , vol.20 , pp. 664-674
    • Legendre, M.1    Audic, S.2    Poirot, O.3    Hingamp, P.4    Seltzer, V.5
  • 20
    • 0037461350 scopus 로고    scopus 로고
    • Inter-domain redox communication in flavoenzymes of the quiescin/sulfhydryl oxidase family: role of a thioredoxin domain in disulfide bond formation
    • Raje S, Thorpe C, (2003) Inter-domain redox communication in flavoenzymes of the quiescin/sulfhydryl oxidase family: role of a thioredoxin domain in disulfide bond formation. Biochem 42: 4560-4568.
    • (2003) Biochem , vol.42 , pp. 4560-4568
    • Raje, S.1    Thorpe, C.2
  • 21
    • 42449098493 scopus 로고    scopus 로고
    • Human quiescin-sulfhydryl oxidase, QSOX1: probing internal redox steps by mutagenesis
    • Heckler EJ, Alon A, Fass D, Thorpe C, (2008) Human quiescin-sulfhydryl oxidase, QSOX1: probing internal redox steps by mutagenesis. Biochem 47: 4955-4963.
    • (2008) Biochem , vol.47 , pp. 4955-4963
    • Heckler, E.J.1    Alon, A.2    Fass, D.3    Thorpe, C.4
  • 22
    • 84865123844 scopus 로고    scopus 로고
    • The dynamic disulphide relay of quiescin sulfhydryl oxidase
    • Alon A, Grossman I, Gat Y, Kodali VK, DiMaio F, et al. (2012) The dynamic disulphide relay of quiescin sulfhydryl oxidase. Nature 488: 414-418.
    • (2012) Nature , vol.488 , pp. 414-418
    • Alon, A.1    Grossman, I.2    Gat, Y.3    Kodali, V.K.4    DiMaio, F.5
  • 23
    • 0034610226 scopus 로고    scopus 로고
    • Vaccinia virus E10R protein is associated with the membranes of intracellular mature virions and has a role in morphogenesis
    • Senkevich TG, Weisberg AS, Moss B, (2000) Vaccinia virus E10R protein is associated with the membranes of intracellular mature virions and has a role in morphogenesis. Virol 278: 244-252.
    • (2000) Virol , vol.278 , pp. 244-252
    • Senkevich, T.G.1    Weisberg, A.S.2    Moss, B.3
  • 24
    • 33645239489 scopus 로고    scopus 로고
    • African Swine Fever Virus pB119L protein is a flavin adenine dinucleotide-linked sulfhydryl oxidase
    • Rodríguez I, Redrejo-Rodríguez M, Rodríguez JM, Alejo A, Salas J, et al. (2006) African Swine Fever Virus pB119L protein is a flavin adenine dinucleotide-linked sulfhydryl oxidase. J Virol 80: 3157-3166.
    • (2006) J Virol , vol.80 , pp. 3157-3166
    • Rodríguez, I.1    Redrejo-Rodríguez, M.2    Rodríguez, J.M.3    Alejo, A.4    Salas, J.5
  • 25
    • 78649444830 scopus 로고    scopus 로고
    • Autographa californica multiple nucleopolyhedrovirus core gene ac92 (p33) is required for efficient budded virus production
    • Nie Y, Fang M, Theilmann DA, (2011) Autographa californica multiple nucleopolyhedrovirus core gene ac92 (p33) is required for efficient budded virus production. Virol 409: 38-45.
    • (2011) Virol , vol.409 , pp. 38-45
    • Nie, Y.1    Fang, M.2    Theilmann, D.A.3
  • 26
    • 77956184308 scopus 로고    scopus 로고
    • Applications of the Restriction Free (RF) cloning procedure for molecular manipulations and protein expression
    • Unger T, Jacobovitch Y, Dantes A, Bernheim R, Peleg Y, (2010) Applications of the Restriction Free (RF) cloning procedure for molecular manipulations and protein expression. J Struct Biol 172: 34-44.
    • (2010) J Struct Biol , vol.172 , pp. 34-44
    • Unger, T.1    Jacobovitch, Y.2    Dantes, A.3    Bernheim, R.4    Peleg, Y.5
  • 27
    • 0027439390 scopus 로고
    • Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin
    • Van Duyne GD, Standaert RF, Karplus PA, Schreiber SL, Clardy J, (1993) Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin. J Mol Biol 229: 105-124.
    • (1993) J Mol Biol , vol.229 , pp. 105-124
    • Van Duyne, G.D.1    Standaert, R.F.2    Karplus, P.A.3    Schreiber, S.L.4    Clardy, J.5
  • 29
    • 33644875355 scopus 로고    scopus 로고
    • Scaling and assessment of data quality
    • Evans PR, (2005) Scaling and assessment of data quality. Acta Crystallogr D 62: 72-82.
    • (2005) Acta Crystallogr D , vol.62 , pp. 72-82
    • Evans, P.R.1
  • 31
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P, Cowtan K, (2005) Coot: model-building tools for molecular graphics. Acta Crystallogr D 60: 2126-2132.
    • (2005) Acta Crystallogr D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 32
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: a new software suite for macromolecular structure determination
    • Brunger AT, Adams PD, Clore GM, DeLano WL, Gros P, et al. (1998) Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr D 54: 905-921.
    • (1998) Acta Crystallogr D , vol.54 , pp. 905-921
    • Brunger, A.T.1    Adams, P.D.2    Clore, G.M.3    DeLano, W.L.4    Gros, P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.